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Reviewed, UniProtKB/Swiss-Prot P24552 (OXDA_FUSSO)

Last modified November 24, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    D-amino-acid oxidase
      Short name=DAMOX
      Short name=DAAO
      Short name=DAO
    EC=1.4.3.3
OrganismFusarium solani subsp. pisi (Nectria haematococca)
Taxonomic identifier70791 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Nectriaceae › Nectria › Nectria haematococca complex

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Protein attributes

Sequence length361 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

This enzyme can effectively convert cephalosporin C into 7-beta-(5-carboxy-5-oxopentanamido)-cephalosporinic acid.

Catalytic activity

A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2.

Cofactor

FAD.

Subcellular location

Peroxisome Potential.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the DAMOX/DASOX family.

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Ontologies

Keywords
   Cellular componentPeroxisome
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionD-amino-acid oxidase activity

Inferred from electronic annotation. Source: EC

binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 361361D-amino-acid oxidase
PRO_0000162766

Regions

Nucleotide binding5 – 1915FAD By similarity
Nucleotide binding34 – 352FAD By similarity
Nucleotide binding45 – 462FAD By similarity
Nucleotide binding50 – 523FAD By similarity
Nucleotide binding332 – 3365FAD By similarity
Motif359 – 3613Microbody targeting signal Potential

Sites

Binding site1721FAD; via amide nitrogen and carbonyl oxygen By similarity
Binding site1951FAD By similarity
Binding site2421Substrate By similarity
Binding site3051Substrate By similarity
Binding site3331Substrate; via carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
P24552-1 [UniParc].

Last modified March 1, 1992. Version 1.
Checksum: 148119480E2A67A5

FASTA36139,696
        10         20         30         40         50         60 
MSNTIVVVGA GVIGLTSALL LSKNKGNKIT VVAKHMPGDY DVEYASPFAG ANHSPMATEE 

        70         80         90        100        110        120 
SSEWERRTWY EFKRLVEEVP EAGVHFQKSR IQRRNVDTEK AQRSGFPDAL FSKEPWFKNM 

       130        140        150        160        170        180 
FEDFREQHPS EVIPGYDSGC EFTSVCINTA IYLPWLLGQC IKNGVIVKRA ILNDISEAKK 

       190        200        210        220        230        240 
LSHAGKTPNI IVNATGLGSY KLGGVEDKTM APARGQIVVV RNESSPMLLT SGVEDGGADV 

       250        260        270        280        290        300 
MYLMQRAAGG GTILGGTYDV GNWESQPDPN IANRIMQRIV EVRPEIANGK GVKGLSVIRH 

       310        320        330        340        350        360 
AVGMRPWRKD GVRIEEEKLD DETWIVHNYG HSGWGYQGSY GCAENVVQLV DKVGKAAKSK 


L

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References

[1]"Structure and expression of cDNA for D-amino acid oxidase active against cephalosporin C from Fusarium solani."
Isogai T., Ono H., Ishitani Y., Kojo H., Ueda Y., Kohsaka M.
J. Biochem. 108:1063-1069(1990) [PubMed: 1982443] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: M-0718 / FERM P-2688.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D00809 mRNA. Translation: BAA00692.1.
PIRJX0152.

3D structure databases

ModBaseSearch...

Family and domain databases

InterProIPR006181. D-amino_acid_oxidase_CS.
IPR006076. FAD-dep_OxRdtase.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF01266. DAO. 1 hit.
[Graphical view]
PROSITEPS00677. DAO. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameOXDA_FUSSO
AccessionPrimary (citable) accession number: P24552
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: March 1, 1992
Last modified: November 24, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents